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Conserved domains on  [gi|118484728|gb|ABK94233|]
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unknown [Populus trichocarpa]

Protein Classification

ubiquitin-fold modifier-conjugating enzyme 1( domain architecture ID 10554693)

ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) is an E1-like enzyme which specifically catalyzes the second step in ufmylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UFC1 pfam08694
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational ...
 8-163 1.83e-117

Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational modifiers are covalently linked to most, if not all, target protein(s) through an enzymatic cascade analogous to ubiquitylation, consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. Ubiquitin-fold modifier 1 (Ufm1) a ubiquitin-like protein is activated by a novel E1-like enzyme, Uba5, by forming a high-energy thioester bond. Activated Ufm1 is then transferred to its cognate E2-like enzyme, Ufc1, in a similar thioester linkage. This family represents the E2-like enzyme.


:

Pssm-ID: 400850  Cd Length: 155  Bit Score: 328.87  E-value: 1.83e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118484728    8 TKSTLTQIPLLTTKAGPRDGAAWTTRLKEEYKALIAYTQMNKSNDNDWFRISSaNPEGTRWTGKCWYVHNLLKYEFDLQF 87
Cdd:pfam08694   1 TKSTVEKIPLLKTKAGPRDGDKWVQRLKEEYAALIKYVENNKENDNDWFRIES-NKEGTRWFGKCWYVHNLLKYEFDLEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118484728   88 DIPVTYPSTAPELELPQLDGKTQKMYRGGKICLTVHFKPLWAKNCPRFGIAHALCLGLAPWLAAEVPVLVDSGMIK 163
Cdd:pfam08694  80 DIPVTYPATPPEIALPELDGKTAKMYRGGKICLTIHFKPLWARNVPKFGIAHALALGLAPWLAAEVPDLVEKGVIK 155
 
Name Accession Description Interval E-value
UFC1 pfam08694
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational ...
 8-163 1.83e-117

Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational modifiers are covalently linked to most, if not all, target protein(s) through an enzymatic cascade analogous to ubiquitylation, consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. Ubiquitin-fold modifier 1 (Ufm1) a ubiquitin-like protein is activated by a novel E1-like enzyme, Uba5, by forming a high-energy thioester bond. Activated Ufm1 is then transferred to its cognate E2-like enzyme, Ufc1, in a similar thioester linkage. This family represents the E2-like enzyme.


Pssm-ID: 400850  Cd Length: 155  Bit Score: 328.87  E-value: 1.83e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118484728    8 TKSTLTQIPLLTTKAGPRDGAAWTTRLKEEYKALIAYTQMNKSNDNDWFRISSaNPEGTRWTGKCWYVHNLLKYEFDLQF 87
Cdd:pfam08694   1 TKSTVEKIPLLKTKAGPRDGDKWVQRLKEEYAALIKYVENNKENDNDWFRIES-NKEGTRWFGKCWYVHNLLKYEFDLEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118484728   88 DIPVTYPSTAPELELPQLDGKTQKMYRGGKICLTVHFKPLWAKNCPRFGIAHALCLGLAPWLAAEVPVLVDSGMIK 163
Cdd:pfam08694  80 DIPVTYPATPPEIALPELDGKTAKMYRGGKICLTIHFKPLWARNVPKFGIAHALALGLAPWLAAEVPDLVEKGVIK 155
UBCc_UFC1 cd11686
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold ...
 9-160 2.28e-117

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) and related proteins; UFC1, also known as Ufm1-conjugating enzyme 1, participates in a ubiquitin-like (UBL) post translation modification enzymatic cascade known as UFMylation, that allows modification by a UBL-type modifier named ubiquitin-fold modifier (UFM1). UBLs are covalently attached to the target proteins or phospholipids through reaction cascades in a manner similar to the ubiquitination pathway. The UFMylation cascade consists of the ubiquitin-like modifier-activating enzyme (UBA5, an E1-like enzyme), UFM1-conjugating enzyme 1 (UFC1, an E2-like enzyme), and the UFM1-specific ligase (UFL1, an E3-like enzyme). UFM1 is synthesized in a precursor form which is then cleaved at the C-terminus to expose a Gly residue. The mature UFM1 is then activated by UBA5, then transferred to UFC1, and finally UFM1 is covalently conjugated with the target protein via UFL1.


Pssm-ID: 467409  Cd Length: 151  Bit Score: 328.41  E-value: 2.28e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118484728   9 KSTLTQIPLLTTKAGPRDGAAWTTRLKEEYKALIAYTQMNKSNDNDWFRISSaNPEGTRWTGKCWYVHNLLKYEFDLQFD 88
Cdd:cd11686    1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIES-NKEGTRWFGKCWYIHNLLKYEFDLEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118484728  89 IPVTYPSTAPELELPQLDGKTQKMYRGGKICLTVHFKPLWAKNCPRFGIAHALCLGLAPWLAAEVPVLVDSG 160
Cdd:cd11686   80 IPVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWLAAEIPDLVEKG 151
 
Name Accession Description Interval E-value
UFC1 pfam08694
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational ...
 8-163 1.83e-117

Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like (UBL) post-translational modifiers are covalently linked to most, if not all, target protein(s) through an enzymatic cascade analogous to ubiquitylation, consisting of E1 (activating), E2 (conjugating), and E3 (ligating) enzymes. Ubiquitin-fold modifier 1 (Ufm1) a ubiquitin-like protein is activated by a novel E1-like enzyme, Uba5, by forming a high-energy thioester bond. Activated Ufm1 is then transferred to its cognate E2-like enzyme, Ufc1, in a similar thioester linkage. This family represents the E2-like enzyme.


Pssm-ID: 400850  Cd Length: 155  Bit Score: 328.87  E-value: 1.83e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118484728    8 TKSTLTQIPLLTTKAGPRDGAAWTTRLKEEYKALIAYTQMNKSNDNDWFRISSaNPEGTRWTGKCWYVHNLLKYEFDLQF 87
Cdd:pfam08694   1 TKSTVEKIPLLKTKAGPRDGDKWVQRLKEEYAALIKYVENNKENDNDWFRIES-NKEGTRWFGKCWYVHNLLKYEFDLEF 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118484728   88 DIPVTYPSTAPELELPQLDGKTQKMYRGGKICLTVHFKPLWAKNCPRFGIAHALCLGLAPWLAAEVPVLVDSGMIK 163
Cdd:pfam08694  80 DIPVTYPATPPEIALPELDGKTAKMYRGGKICLTIHFKPLWARNVPKFGIAHALALGLAPWLAAEVPDLVEKGVIK 155
UBCc_UFC1 cd11686
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold ...
 9-160 2.28e-117

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain of ubiquitin-fold modifier-conjugating enzyme 1 (UFC1) and related proteins; UFC1, also known as Ufm1-conjugating enzyme 1, participates in a ubiquitin-like (UBL) post translation modification enzymatic cascade known as UFMylation, that allows modification by a UBL-type modifier named ubiquitin-fold modifier (UFM1). UBLs are covalently attached to the target proteins or phospholipids through reaction cascades in a manner similar to the ubiquitination pathway. The UFMylation cascade consists of the ubiquitin-like modifier-activating enzyme (UBA5, an E1-like enzyme), UFM1-conjugating enzyme 1 (UFC1, an E2-like enzyme), and the UFM1-specific ligase (UFL1, an E3-like enzyme). UFM1 is synthesized in a precursor form which is then cleaved at the C-terminus to expose a Gly residue. The mature UFM1 is then activated by UBA5, then transferred to UFC1, and finally UFM1 is covalently conjugated with the target protein via UFL1.


Pssm-ID: 467409  Cd Length: 151  Bit Score: 328.41  E-value: 2.28e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118484728   9 KSTLTQIPLLTTKAGPRDGAAWTTRLKEEYKALIAYTQMNKSNDNDWFRISSaNPEGTRWTGKCWYVHNLLKYEFDLQFD 88
Cdd:cd11686    1 KKTVAKIPLLTTRAGPRDGDLWIQRLKEEYQALIKYVENNKEADNDWFRIES-NKEGTRWFGKCWYIHNLLKYEFDLEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118484728  89 IPVTYPSTAPELELPQLDGKTQKMYRGGKICLTVHFKPLWAKNCPRFGIAHALCLGLAPWLAAEVPVLVDSG 160
Cdd:cd11686   80 IPVTYPTTPPEIALPELDGKTAKMYRGGKICLTVHFKPLWARNVPKFGIAHALALGLGPWLAAEIPDLVEKG 151
UBCc_UEV cd00195
Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; ...
 33-128 1.42e-04

Ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain/ubiquitin E2 variant (UEV) domain; The family includes ubiquitin-conjugating enzyme E2, catalytic (UBCc) domain and ubiquitin (Ub) E2 variant (UEV) domain. They belong to the ubiquitin-conjugating (UBC) superfamily that represents a structural domain with an alpha-beta(4)-alpha(3) core fold. E2 is part of the ubiquitin-mediated protein degradation pathway in which a thioester linkage forms between a conserved cysteine and the C-terminus of ubiquitin, and complexes with ubiquitin protein ligase enzymes, E3. This pathway regulates many fundamental cellular processes. There are also other E2s which form thioester linkages without the use of E3s. Several UBC homologs (TSG101, Mms2, Croc-1 and similar proteins) contains the UEV domain, which lacks the active site cysteine essential for ubiquitination and appear to function in DNA repair pathways.


Pssm-ID: 467407 [Multi-domain]  Cd Length: 112  Bit Score: 39.59  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118484728  33 RLKEEYKALiaytqmnKSNDNDWFRISSANPEGTRWTGKCWYVHNLLkYE---FDLQFDIPVTYPSTAPELELpqldgkT 109
Cdd:cd00195    2 RLQKELKEL-------QKNPPPGISVEPVDDDLFHWKATIKGPEGTP-YEggvFKLDIEFPDDYPFKPPKVRF------L 67

                         90       100
                 ....*....|....*....|....
gi 118484728 110 QKMY-----RGGKICLTVHFKPLW 128
Cdd:cd00195   68 TPIYhpnvdPDGEICLDILKSEGW 91
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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